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P53397 (OGG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-glycosylase/DNA lyase

Including the following 2 domains:

  1. 8-oxoguanine DNA glycosylase
    EC=3.2.2.-
  2. DNA-(apurinic or apyrimidinic site) lyase
    Short name=AP lyase
    EC=4.2.99.18
Gene names
Name:OGG1
Ordered Locus Names:YML060W
ORF Names:YM9958.02
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

Subcellular location

Nucleus.

Miscellaneous

Present with 3690 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the type-1 OGG1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376N-glycosylase/DNA lyase
PRO_0000058595

Sites

Active site2411Schiff-base intermediate with DNA
Binding site1341DNA By similarity
Binding site1391DNA By similarity
Binding site1891DNA By similarity
Binding site25818-oxoguanine; via carbonyl oxygen By similarity
Binding site26018-oxoguanine By similarity
Binding site2621DNA By similarity
Binding site32018-oxoguanine By similarity
Binding site32418-oxoguanine By similarity

Experimental info

Mutagenesis2411K → Q: Abolishes both DNA glycosylase and AP lyase activity. Ref.4 Ref.5
Mutagenesis2411K → R: Diminishes both DNA glycosylase and AP lyase activity. Ref.4 Ref.5

Sequences

Sequence LengthMass (Da)Tools
P53397 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4ADB72EB20E4BF20

FASTA37642,781
        10         20         30         40         50         60 
MSYKFGKLAI NKSELCLANV LQAGQSFRWI WDEKLNQYST TMKIGQQEKY SVVILRQDEE 

        70         80         90        100        110        120 
NEILEFVAVG DCGNQDALKT HLMKYFRLDV SLKHLFDNVW IPSDKAFAKL SPQGIRILAQ 

       130        140        150        160        170        180 
EPWETLISFI CSSNNNISRI TRMCNSLCSN FGNLITTIDG VAYHSFPTSE ELTSRATEAK 

       190        200        210        220        230        240 
LRELGFGYRA KYIIETARKL VNDKAEANIT SDTTYLQSIC KDAQYEDVRE HLMSYNGVGP 

       250        260        270        280        290        300 
KVADCVCLMG LHMDGIVPVD VHVSRIAKRD YQISANKNHL KELRTKYNAL PISRKKINLE 

       310        320        330        340        350        360 
LDHIRLMLFK KWGSYAGWAQ GVLFSKEIGG TSGSTTTGTI KKRKWDMIKE TEAIVTKQMK 

       370 
LKVELSDLHI KEAKID 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine."
van der Kemp P.A., Thomas D., Barbey R., de Oliveira R., Boiteux S.
Proc. Natl. Acad. Sci. U.S.A. 93:5197-5202(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The Ogg1 protein of Saccharomyces cerevisiae: a 7,8-dihydro-8-oxoguanine DNA glycosylase/AP lyase whose lysine 241 is a critical residue for catalytic activity."
Girard P.-M., Guibourt N., Boiteux S.
Nucleic Acids Res. 25:3204-3211(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-241.
[5]"Catalytic and DNA binding properties of the ogg1 protein of Saccharomyces cerevisiae: comparison between the wild type and the K241R and K241Q active-site mutant proteins."
Guibourt N., Castaing B., Van Der Kemp P.A., Boiteux S.
Biochemistry 39:1716-1724(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-241.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U44855 Genomic DNA. Translation: AAC49312.1.
Z46729 Genomic DNA. Translation: CAA86715.1.
BK006946 Genomic DNA. Translation: DAA09837.1.
PIRS49801.
RefSeqNP_013651.1. NM_001182419.1.

3D structure databases

ProteinModelPortalP53397.
SMRP53397. Positions 12-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35106. 38 interactions.
DIPDIP-4538N.
MINTMINT-566071.
STRING4932.YML060W.

Proteomic databases

MaxQBP53397.
PaxDbP53397.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML060W; YML060W; YML060W.
GeneID854942.
KEGGsce:YML060W.

Organism-specific databases

CYGDYML060w.
SGDS000004525. OGG1.

Phylogenomic databases

eggNOGCOG0122.
GeneTreeENSGT00640000091554.
HOGENOMHOG000180756.
KOK03660.
OMASELCLAN.
OrthoDBEOG7TQV9T.

Enzyme and pathway databases

BioCycYEAST:G3O-32655-MONOMER.

Gene expression databases

GenevestigatorP53397.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
InterProIPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
IPR004577. Ogg.
IPR012904. OGG_N.
[Graphical view]
PfamPF00730. HhH-GPD. 1 hit.
PF07934. OGG_N. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
TIGRFAMsTIGR00588. ogg. 1 hit.
ProtoNetSearch...

Other

NextBio977995.
PROP53397.

Entry information

Entry nameOGG1_YEAST
AccessionPrimary (citable) accession number: P53397
Secondary accession number(s): D6VZB3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families